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P09110

- THIK_HUMAN

UniProt

P09110 - THIK_HUMAN

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Protein

3-ketoacyl-CoA thiolase, peroxisomal

Gene

ACAA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei123 – 1231Acyl-thioester intermediateBy similarity
Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotation
Active sitei408 – 4081Proton acceptorPROSITE-ProRule annotation

GO - Molecular functioni

  1. acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC
  2. palmitoyl-CoA oxidase activity Source: UniProtKB

GO - Biological processi

  1. alpha-linolenic acid metabolic process Source: Reactome
  2. bile acid metabolic process Source: UniProtKB
  3. cellular lipid metabolic process Source: Reactome
  4. fatty acid beta-oxidation Source: UniProtKB
  5. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. unsaturated fatty acid metabolic process Source: Reactome
  8. very long-chain fatty acid metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS00752-MONOMER.
ReactomeiREACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17062. Beta-oxidation of very long chain fatty acids.
UniPathwayiUPA00199.

Names & Taxonomyi

Protein namesi
Recommended name:
3-ketoacyl-CoA thiolase, peroxisomal (EC:2.3.1.16)
Alternative name(s):
Acetyl-CoA acyltransferase
Beta-ketothiolase
Peroxisomal 3-oxoacyl-CoA thiolase
Gene namesi
Name:ACAA1
Synonyms:ACAA, PTHIO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:82. ACAA1.

Subcellular locationi

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. membrane Source: UniProtKB
  3. peroxisomal matrix Source: Reactome
  4. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626PeroxisomeAdd
BLAST
Chaini27 – 4243983-ketoacyl-CoA thiolase, peroxisomalPRO_0000034067Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei59 – 591Phosphothreonine1 Publication
Modified residuei60 – 601Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP09110.
PaxDbiP09110.
PeptideAtlasiP09110.
PRIDEiP09110.

2D gel databases

REPRODUCTION-2DPAGEIPI00012828.
UCD-2DPAGEP09110.

PTM databases

PhosphoSiteiP09110.

Expressioni

Inductioni

Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

Gene expression databases

BgeeiP09110.
CleanExiHS_ACAA1.
ExpressionAtlasiP09110. baseline and differential.
GenevestigatoriP09110.

Organism-specific databases

HPAiHPA006764.
HPA007244.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi106548. 24 interactions.
IntActiP09110. 1 interaction.
MINTiMINT-3006670.
STRINGi9606.ENSP00000333664.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 458
Turni51 – 533
Turni55 – 584
Helixi61 – 7616
Helixi80 – 823
Beta strandi86 – 894
Beta strandi91 – 944
Helixi95 – 973
Helixi98 – 10710
Beta strandi116 – 1205
Helixi122 – 1243
Helixi125 – 13814
Beta strandi143 – 15210
Turni153 – 1553
Helixi168 – 1703
Helixi172 – 1754
Helixi176 – 1783
Helixi181 – 19111
Helixi196 – 21621
Turni217 – 2226
Beta strandi226 – 2316
Beta strandi237 – 2426
Helixi254 – 2596
Beta strandi263 – 2653
Beta strandi279 – 28911
Helixi290 – 2967
Beta strandi302 – 31110
Helixi314 – 3196
Helixi320 – 33213
Helixi336 – 3383
Beta strandi339 – 3446
Helixi349 – 35911
Helixi363 – 3653
Helixi372 – 3754
Turni379 – 3813
Helixi382 – 39716
Beta strandi401 – 4099
Turni410 – 4123
Beta strandi413 – 4219

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IIKX-ray2.55A/B30-423[»]
ProteinModelPortaliP09110.
SMRiP09110. Positions 28-424.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09110.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0183.
GeneTreeiENSGT00760000119318.
HOGENOMiHOG000012239.
HOVERGENiHBG003112.
InParanoidiP09110.
KOiK07513.
OMAiACTREWG.
OrthoDBiEOG7K3TM6.
PhylomeDBiP09110.
TreeFamiTF332308.

Family and domain databases

Gene3Di3.40.47.10. 4 hits.
InterProiIPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view]
PfamiPF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMiSSF53901. SSF53901. 2 hits.
TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEiPS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P09110-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR
60 70 80 90 100
AGRGGFKDTT PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM
110 120 130 140 150
ARIAQFLSDI PETVPLSTVN RQCSSGLQAV ASIAGGIRNG SYDIGMACGV
160 170 180 190 200
ESMSLADRGN PGNITSRLME KEKARDCLIP MGITSENVAE RFGISREKQD
210 220 230 240 250
TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI TVTQDEGIRP
260 270 280 290 300
STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI
310 320 330 340 350
LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS
360 370 380 390 400
QAAYCVEKLR LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR
410 420
AYGVVSMCIG TGMGAAAVFE YPGN
Length:424
Mass (Da):44,292
Last modified:October 1, 1989 - v2
Checksum:i71B2BBAFA06AE412
GO
Isoform 2 (identifier: P09110-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     149-181: Missing.
     272-331: Missing.

Note: No experimental confirmation available.

Show »
Length:331
Mass (Da):34,665
Checksum:i8137A0AC448FBA24
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721E → D.
Corresponds to variant rs156265 [ dbSNP | Ensembl ].
VAR_011904
Natural varianti387 – 3871V → A.1 Publication
Corresponds to variant rs2229528 [ dbSNP | Ensembl ].
VAR_069148

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei149 – 18133Missing in isoform 2. 1 PublicationVSP_046195Add
BLAST
Alternative sequencei272 – 33160Missing in isoform 2. 1 PublicationVSP_046196Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12966 mRNA. Translation: CAA31412.1.
X14813 mRNA. Translation: CAA32918.1.
X65140 Genomic DNA. Translation: CAA46270.1.
X65148 Genomic DNA. Translation: CAA46271.1.
AP006309 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64516.1.
BC000635 mRNA. Translation: AAH00635.1.
BC011977 mRNA. Translation: AAH11977.1.
BC014474 mRNA. Translation: AAH14474.1.
CCDSiCCDS2673.1. [P09110-1]
CCDS46794.1. [P09110-2]
PIRiS17515. XUHUAB.
RefSeqiNP_001123882.1. NM_001130410.1. [P09110-2]
NP_001598.1. NM_001607.3. [P09110-1]
UniGeneiHs.643487.

Genome annotation databases

EnsembliENST00000301810; ENSP00000301810; ENSG00000060971. [P09110-2]
ENST00000333167; ENSP00000333664; ENSG00000060971. [P09110-1]
GeneIDi30.
KEGGihsa:30.
UCSCiuc003cht.3. human. [P09110-1]
uc003chu.3. human.

Polymorphism databases

DMDMi135751.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12966 mRNA. Translation: CAA31412.1 .
X14813 mRNA. Translation: CAA32918.1 .
X65140 Genomic DNA. Translation: CAA46270.1 .
X65148 Genomic DNA. Translation: CAA46271.1 .
AP006309 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64516.1 .
BC000635 mRNA. Translation: AAH00635.1 .
BC011977 mRNA. Translation: AAH11977.1 .
BC014474 mRNA. Translation: AAH14474.1 .
CCDSi CCDS2673.1. [P09110-1 ]
CCDS46794.1. [P09110-2 ]
PIRi S17515. XUHUAB.
RefSeqi NP_001123882.1. NM_001130410.1. [P09110-2 ]
NP_001598.1. NM_001607.3. [P09110-1 ]
UniGenei Hs.643487.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IIK X-ray 2.55 A/B 30-423 [» ]
ProteinModelPortali P09110.
SMRi P09110. Positions 28-424.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106548. 24 interactions.
IntActi P09110. 1 interaction.
MINTi MINT-3006670.
STRINGi 9606.ENSP00000333664.

PTM databases

PhosphoSitei P09110.

Polymorphism databases

DMDMi 135751.

2D gel databases

REPRODUCTION-2DPAGE IPI00012828.
UCD-2DPAGE P09110.

Proteomic databases

MaxQBi P09110.
PaxDbi P09110.
PeptideAtlasi P09110.
PRIDEi P09110.

Protocols and materials databases

DNASUi 30.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000301810 ; ENSP00000301810 ; ENSG00000060971 . [P09110-2 ]
ENST00000333167 ; ENSP00000333664 ; ENSG00000060971 . [P09110-1 ]
GeneIDi 30.
KEGGi hsa:30.
UCSCi uc003cht.3. human. [P09110-1 ]
uc003chu.3. human.

Organism-specific databases

CTDi 30.
GeneCardsi GC03M038164.
HGNCi HGNC:82. ACAA1.
HPAi HPA006764.
HPA007244.
MIMi 604054. gene.
neXtProti NX_P09110.
PharmGKBi PA24419.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0183.
GeneTreei ENSGT00760000119318.
HOGENOMi HOG000012239.
HOVERGENi HBG003112.
InParanoidi P09110.
KOi K07513.
OMAi ACTREWG.
OrthoDBi EOG7K3TM6.
PhylomeDBi P09110.
TreeFami TF332308.

Enzyme and pathway databases

UniPathwayi UPA00199 .
BioCyci MetaCyc:HS00752-MONOMER.
Reactomei REACT_121147. alpha-linolenic acid (ALA) metabolism.
REACT_17062. Beta-oxidation of very long chain fatty acids.

Miscellaneous databases

ChiTaRSi ACAA1. human.
EvolutionaryTracei P09110.
GeneWikii ACAA1.
GenomeRNAii 30.
NextBioi 107.
PROi P09110.
SOURCEi Search...

Gene expression databases

Bgeei P09110.
CleanExi HS_ACAA1.
ExpressionAtlasi P09110. baseline and differential.
Genevestigatori P09110.

Family and domain databases

Gene3Di 3.40.47.10. 4 hits.
InterProi IPR002155. Thiolase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
IPR020615. Thiolase_acyl_enz_int_AS.
IPR020610. Thiolase_AS.
IPR020617. Thiolase_C.
IPR020613. Thiolase_CS.
IPR020616. Thiolase_N.
[Graphical view ]
Pfami PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
SUPFAMi SSF53901. SSF53901. 2 hits.
TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
PROSITEi PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase."
    Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.
    Nucleic Acids Res. 16:10369-10369(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. Bout A.
    Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 285-287.
  3. "Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase."
    Fairbairn L.J., Tanner M.J.A.
    Nucleic Acids Res. 17:3588-3588(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  4. "Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient."
    Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.
    Biochim. Biophys. Acta 1090:43-51(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-387.
    Tissue: Lymph, Ovary and Pancreas.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Crystal structure of human peroxisomal acetyl-COA acyl transferase 1 (ACAA1)."
    Structural genomics consortium (SGC)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, SUBUNIT.

Entry informationi

Entry nameiTHIK_HUMAN
AccessioniPrimary (citable) accession number: P09110
Secondary accession number(s): G5E935, Q96CA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1989
Last modified: October 29, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3